ThermoLink: Bridging disulfide bonds and enzyme thermostability through database construction and machine learning prediction

热稳定性 化学 蛋白质二硫键异构酶 半胱氨酸 共价键 蛋白质工程 蛋白质折叠 二硫键 组合化学 生物化学 有机化学
作者
Ran Xu,Q C Pan,Guoliang Zhu,Yilin Ye,Xin Min,Zechen Wang,Sheng Wang,Weifeng Li,Yanjie Wei,Jingjing Guo,Liangzhen Zheng
出处
期刊:Protein Science [Wiley]
卷期号:33 (9)
标识
DOI:10.1002/pro.5097
摘要

Abstract Disulfide bonds, covalently formed by sulfur atoms in cysteine residues, play a crucial role in protein folding and structure stability. Considering their significance, artificial disulfide bonds are often introduced to enhance protein thermostability. Although an increasing number of tools can assist with this task, significant amounts of time and resources are often wasted owing to inadequate consideration. To enhance the accuracy and efficiency of designing disulfide bonds for protein thermostability improvement, we initially collected disulfide bond and protein thermostability data from extensive literature sources. Thereafter, we extracted various sequence‐ and structure‐based features and constructed machine‐learning models to predict whether disulfide bonds can improve protein thermostability. Among all models, the neighborhood context model based on the Adaboost‐DT algorithm performed the best, yielding “area under the receiver operating characteristic curve” and accuracy scores of 0.773 and 0.714, respectively. Furthermore, we also found AlphaFold2 to exhibit high superiority in predicting disulfide bonds, and to some extent, the coevolutionary relationship between residue pairs potentially guided artificial disulfide bond design. Moreover, several mutants of imine reductase 89 (IR89) with artificially designed thermostable disulfide bonds were experimentally proven to be considerably efficient for substrate catalysis. The SS‐bond data have been integrated into an online server, namely, ThermoLink, available at guolab.mpu.edu.mo/thermoLink .
最长约 10秒,即可获得该文献文件

科研通智能强力驱动
Strongly Powered by AbleSci AI
更新
大幅提高文件上传限制,最高150M (2024-4-1)

科研通是完全免费的文献互助平台,具备全网最快的应助速度,最高的求助完成率。 对每一个文献求助,科研通都将尽心尽力,给求助人一个满意的交代。
实时播报
小奕完成签到,获得积分10
1秒前
1秒前
liuchao完成签到,获得积分10
2秒前
Tim完成签到 ,获得积分10
2秒前
3秒前
暮光之城完成签到,获得积分10
4秒前
ZJY完成签到,获得积分20
5秒前
云fly发布了新的文献求助10
7秒前
无私的朝雪完成签到 ,获得积分10
7秒前
weizheng完成签到,获得积分0
8秒前
星宇完成签到 ,获得积分10
9秒前
xc完成签到,获得积分10
9秒前
Jasper应助ZJY采纳,获得10
11秒前
无辜玉米完成签到 ,获得积分10
13秒前
大海是故乡完成签到,获得积分10
14秒前
云fly完成签到,获得积分10
14秒前
14秒前
叉叉茶完成签到,获得积分10
15秒前
九月完成签到 ,获得积分10
15秒前
孩子们我回来了完成签到,获得积分10
16秒前
drift完成签到,获得积分10
16秒前
哈哈完成签到 ,获得积分10
16秒前
中中中发布了新的文献求助20
17秒前
一支小玫瑰完成签到 ,获得积分10
19秒前
小明完成签到,获得积分10
19秒前
苏钰完成签到,获得积分10
19秒前
Akim应助孩子们我回来了采纳,获得10
21秒前
懵懂的梦秋完成签到,获得积分10
21秒前
姆姆没买完成签到 ,获得积分10
21秒前
典雅的毛巾完成签到 ,获得积分10
22秒前
clock完成签到 ,获得积分10
23秒前
xiangwang完成签到 ,获得积分10
23秒前
lizh187完成签到 ,获得积分10
24秒前
努力找文献完成签到,获得积分10
28秒前
会飞的猪完成签到 ,获得积分10
29秒前
木月月复习了嘛完成签到,获得积分10
30秒前
hmj007完成签到,获得积分10
30秒前
稳重的蜡烛完成签到,获得积分10
32秒前
摇不滚摇滚完成签到 ,获得积分10
32秒前
冷傲的丹雪完成签到 ,获得积分10
32秒前
高分求助中
The ACS Guide to Scholarly Communication 2500
Sustainability in Tides Chemistry 2000
Studien zur Ideengeschichte der Gesetzgebung 1000
TM 5-855-1(Fundamentals of protective design for conventional weapons) 1000
Threaded Harmony: A Sustainable Approach to Fashion 810
Pharmacogenomics: Applications to Patient Care, Third Edition 800
Gerard de Lairesse : an artist between stage and studio 500
热门求助领域 (近24小时)
化学 医学 生物 材料科学 工程类 有机化学 生物化学 物理 内科学 纳米技术 计算机科学 化学工程 复合材料 基因 遗传学 催化作用 物理化学 免疫学 量子力学 细胞生物学
热门帖子
关注 科研通微信公众号,转发送积分 3081618
求助须知:如何正确求助?哪些是违规求助? 2734490
关于积分的说明 7533077
捐赠科研通 2384041
什么是DOI,文献DOI怎么找? 1264161
科研通“疑难数据库(出版商)”最低求助积分说明 612567
版权声明 597584